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PreviewIssue DateTitleAuthor(s)
2010The two-faced nature of small heat-shock proteins: Amyloid fibril assembly and the inhibition of fibril formation. Relevance to disease statesEcroyd, H.; Meehan, S.; Carver, J.; Simon, S.; Arrigo, A.
2008Unravelling the mysteries of protein folding and misfoldingEcroyd, H.; Carver, J.
2016The effect of milk constituents and crowding agents on amyloid fibril formation by κ-caseinLiu, J.; Dehle, F.; Liu, Y.; Bahraminejad, E.; Ecroyd, H.; Thorn, D.; Carver, J.
2013Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foodsHolt, C.; Carver, J.; Ecroyd, H.; Thorn, D.
2011Binding of the molecular chaperone alpha B-crystallin to A beta amyloid fibrils Inhibits fibril elongationShammas, S.; Waudby, C.; Wang, S.; Buell, A.; Knowles, T.; Ecroyd, H.; Welland, M.; Carver, J.; Dobson, C.; Meehan, S.
2010The interaction of αB-crystallin with mature α-synuclein amyloid fibrils inhibits their elongationWaudby, C.; Knowles, T.; Devlin, G.; Skepper, J.; Ecroyd, H.; Carver, J.; Welland, M.; Christodoulou, J.; Dobson, C.; Meehan, S.
2008Amyloid fibril formation by bovine milk αs₂-casein occurs under physiological conditions yet is prevented by its natural counterpart, αs₁-caseinThorn, D.; Ecroyd, H.; Sunde, M.; Poon, S.; Carver, J.
2008The effect of small molecules in modulating the chaperone activity of αB-crystallin against ordered and disordered protein aggregationEcroyd, H.; Carver, J.
2009The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compoundsHudson, S.; Ecroyd, H.; Kee, T.; Carver, J.